Catalytic antibody 5C8, free FAB. Determined by X-ray diffraction at 2.5 Å resolution. Released 23 Mar 1999.
Explore 15C8 in 3D Show helices and sheets RCSB PDB PDBe
15C8 contains 16 α-helices and 43 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 6 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 18-25 | 8 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 7 |
| β-strand | 45-52 | 8 | 7 |
| β-strand | 56-59 | 4 | 7 |
| β-strand | 64 | 1 | 6 |
| β-strand | 67-72 | 6 | 6 |
| β-strand | 77-82 | 6 | 6 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 7 |
| β-strand | 103 | 1 | 7 |
| β-strand | 107-111 | 5 | 7 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 8 |
| β-strand | 120-124 | 5 | 9 |
| β-strand | 138-147 | 10 | 9 |
| β-strand | 148 | 1 | 8 |
| β-strand | 153-157 | 4 | 10 |
| α-helix | 162-164 | 3 | |
| β-strand | 166 | 1 | 10 |
| β-strand | 171-173 | 3 | 9 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-179 | 3 | 9 |
| β-strand | 184-193 | 10 | 9 |
| β-strand | 206-212 | 6 | 10 |
| α-helix | 213-215 | 3 | |
| β-strand | 217-222 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-28 | 11 | 1 |
| α-helix | 30-32 | 3 | |
| β-strand | 33-38 | 6 | 2 |
| α-helix | 43-44 | 2 | |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-75 | 14 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 3 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 153-155 | 3 | 5 |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 165 | 1 | |
| α-helix | 167 | 1 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 5 |
| β-strand | 205-210 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IgG 5C8 FAB (light chain) | L | protein | 213 | Mus musculus | P01837 (AlphaFold model) |
| IgG 5C8 FAB (heavy chain) | H | protein | 217 | Mus musculus | P01869 (AlphaFold model) |
>15C8_1 IGG 5C8 FAB (LIGHT CHAIN) (chains L) DIVLTQSPAIMSASLGERVTMTCTASSSVSSSNLHWYQQKPGSSPKLWIYSTSNLASGVP ARFSGSGSGTSYSLTISSMEAEDAATYYCHQYHRSPYTFGGGTKLEIKRADAAPTVSIFP PSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTL TLTKDEYERHNSYTCEATHKTSTSPIVKSFNRN
>15C8_2 IGG 5C8 FAB (HEAVY CHAIN) (chains H) EVQLQQSGAELVKPGASVKLSCTASGFNIKDTYMHWVKQKPEQGLEWIAQIDPANGNTKY DPKFQGKATITADTSSNTAYLHLSSLTSEDSAVYYCAADPPYYGHGDYWGQGTTLTVSSA KTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDL YTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIV
Ligand-Induced Conformational Changes in a Catalytic Antibody: Comparison of the Bound and Unbound Structure of Fab 5C8. Gruber, K., Heine, A., Stura, E.A. et al. To be published.
Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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